Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxyxanthones with different prenyl donors by a bisindolyl benzoquinone C- and N-prenyltransferase

Tarcz, Sylwia; Xie, Xiulan; Li, Shu-Ming

doi:10.1039/c4ra00337c

Cited by 12 publications

(10 citation statements)

References 25 publications

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“…Tryptophan and analogs as well as tryptophan-containing cyclic dipeptides were not accepted by this enzyme (Tarcz et al 2014a). However, AstPT used DMAPP, GPP, and FPP for O-prenylation of hydroxyxanthones (Table 5) (Tarcz et al 2014b). AstPT and XptB showed different substrate preferences and regioselectivities toward xanthones.…”

Section: Chemoenzymatic Synthesis Of Prenylated Xanthonesmentioning

confidence: 98%

“…The acceptance of the unnatural DMAPP analogs was also demonstrated with three cyclic dipeptide reverse C3-PTs, AnaPT, CdpNPT, and CdpC3PT (Schuller et al 2012; The data are adopted from publication for AstPT (4.1 μM, 16 h) (Tarcz et al 2014b) n.d. not detected ). All of these enzymes catalyzed the Friedel-Crafts alkylation of cyclic dipeptides.…”

Section: Acceptance Of Unnatural Dmapp Analogs By the Dmats Enzymesmentioning

confidence: 99%

“…In the presence of GPP or FPP, none of the tested indole derivatives including tryptophan and cyclic dipeptides, hydroxynaphthalenes, and flavonoids was accepted by this enzyme. Remarkably, AstPT accepted a number of hydroxyxanthones in the presence of not only DMAPP, but also GPP and FPP and catalyzed Oprenylations at the same position of the benzene ring (Table 9) (Tarcz et al 2014b).…”

Section: Acceptance Of Gpp and Fpp By The Dmats Enzymesmentioning

confidence: 99%

“…FgaPT2 and 5-DMATS were reported to catalyze regiospecific prenylations of indolocarbazoles at the para-position of the indole N-atom, and four prenylated products were obtained. These results expanded not only the potential usage The data are adopted from publication for XptB (3.8 μM, 16 h) (Pockrandt et al 2012) and for AstPT (4.1 μM, 16 h) (Tarcz et al 2014b) n.d. not detected of these enzymes in the structural modification, but also provided leading compounds for further biological research (Fig. 3) (Yu et al 2012a).…”

Section: Chemoenzymatic Synthesis Of Prenylated Indolocarbazolesmentioning

confidence: 99%

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Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology

Fan

Winkelblech

2015

Appl Microbiol Biotechnol

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Prenylated compounds are ubiquitously found in nature and demonstrate interesting biological and pharmacological activities. Prenyltransferases catalyze the attachment of prenyl moieties from different prenyl donors to various acceptors and contribute significantly to the structural and biological diversity of natural products. In the last decade, significant progress has been achieved for the prenyltransferases of the dimethylallyltryptophan synthase (DMATS) superfamily. More than 40 members of these soluble enzymes are identified in microorganisms and characterized biochemically. These enzymes were also successfully used for production of a large number of prenylated derivatives. N1-, C4-, C5-, C6-, and C7-prenylated tryptophan and N1-, C2-, C3-, C4-, and C7-prenylated tryptophan-containing peptides were obtained by using DMATS enzymes as biocatalysts. Tyrosine and xanthone prenyltransferases were used for production of prenylated derivatives of their analogs. More interestingly, the members of the DMATS superfamily demonstrated intriguing substrate and catalytic promiscuity and also used structurally quite different compounds as prenyl acceptors. Prenylated hydroxynaphthalenes, flavonoids, indolocarbazoles, and acylphloroglucinols, which are typical bacterial or plant metabolites, were produced by using several fungal DMATS enzymes. Furthermore, the potential usage of these enzymes was further expanded by using natural or unnatural DMAPP analogs as well as by coexpression with other genes like NRPS and by development of whole cell biocatalyst.

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Section: Chemoenzymatic Synthesis Of Prenylated Xanthonesmentioning

confidence: 98%

Section: Acceptance Of Unnatural Dmapp Analogs By the Dmats Enzymesmentioning

confidence: 99%

Section: Acceptance Of Gpp and Fpp By The Dmats Enzymesmentioning

confidence: 99%

Section: Chemoenzymatic Synthesis Of Prenylated Indolocarbazolesmentioning

confidence: 99%

See 2 more Smart Citations

Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology

Fan

Winkelblech

2015

Appl Microbiol Biotechnol

Self Cite

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“…43,44 Prenylation of the dimers is frequently found in plant-derived xanthones. 45 Pendant sugars are also found as a structural feature of dimers, see for example puniceaside C (72, plant derived) and Hirtusneanoside (120, lichenoid). It is also known that some substituents are removed from the xanthone core, such as the reduction of hydroxyl functions and reductive dearomatisation.…”

Section: Stefanmentioning

confidence: 99%

Xanthone dimers: a compound family which is both common and privileged

2015

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Covering: up to 2014. Xanthone dimers are a widespread, structurally-diverse family of natural products frequently found in plants, fungi and lichens. They feature an intriguing variety of linkages between the component xanthones (benzannulated chromanones). These synthetically elusive secondary metabolites are of great interest due to their broad array of bioactivities, which has led to the xanthones being designated as 'privileged structures'. We seek herein to give an overview of all reliably-described xanthone dimers, their structures, occurrence, and the bioactivities established to date. The possible biosynthetic pathways leading to members of this family are also discussed in light of our current knowledge.

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Enzymatic O‐Prenylation of Diverse Phenolic Compounds by a Permissive O‐Prenyltransferase from the Medicinal Mushroom Antrodia camphorata

Dong

et al. 2019

Adv Synth Catal

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Prenylated compounds are pharmacologically attractive natural products that are widely distributed in nature. Prenyltransferases (PTs) could catalyze the transfer of prenyl moieties to aromatic acceptors and increase the structural diversity and biological activity of natural products. In this work, a permissive O-prenyltransferase AcaPT was discovered from Antrodia camphorata, a precious medicinal mushroom in Taiwan. AcaPT exhibited robust O-prenylation capability toward structurally diverse drug-like phenolic compounds, including antrodins, flavonoids, and coumarins. In total, 23 Oprenylated products were obtained by scaled-up enzymatic synthesis. AcaPT could be used as an efficient biocatalyst to synthesize O-prenylated derivatives for drug discovery.

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Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxyxanthones with different prenyl donors by a bisindolyl benzoquinone C- and N-prenyltransferase

Abstract: Supplied with unnatural substrates like hydroxyxanthones, the C- and N-prenyltransferase AstPT performs O-prenylation using DMAPP, GPP and also FPP as prenyl donor.

Cited by 12 publications

References 25 publications

Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology

Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology

Xanthone dimers: a compound family which is both common and privileged

Enzymatic O‐Prenylation of Diverse Phenolic Compounds by a Permissive O‐Prenyltransferase from the Medicinal Mushroom Antrodia camphorata

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